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Arbitrium is a viral peptide produced by bacteriophages to communicate with each other and decide host cell fate. [1] It is six amino acids (aa) long, and so is also referred to as a hexapeptide. It is produced when a phage infects a bacterial host. and signals to other phages that the host has been infected.
Research in 2017 revealed that the bacteriophage Φ3T makes a short viral protein that signals other bacteriophages to lie dormant instead of killing the host bacterium. Arbitrium is the name given to this protein by the researchers who discovered it. [70] [71]
This protein has nine domains homologous to protease inhibitors. [8] It may also have functions in other tissues and during other stages of development. It is a major proteoglycan component in the glomerular basement membrane and may play a role in the renal filtration and cell-matrix interactions.
Protein is the key to keeping you full and energized. But when it comes to the source, some proteins stand above the rest, according to a new report from an advisory committee to the United States ...
Protein is a nutrient that's essential for muscle growth and maintenance, metabolism regulation, and a healthy immune system. "Protein from steak is particularly favorable," says Bikman, because ...
The words protein, polypeptide, and peptide are a little ambiguous and can overlap in meaning. Protein is generally used to refer to the complete biological molecule in a stable conformation, whereas peptide is generally reserved for a short amino acid oligomers often lacking a stable 3D structure. But the boundary between the two is not well ...
T-complex protein Ring Complex (TRiC), otherwise known as Chaperonin Containing TCP-1 (CCT), [a] is a multiprotein complex and the chaperonin of eukaryotic cells. Like the bacterial GroEL , the TRiC complex aids in the folding of ~10% of the proteome, and actin and tubulin are some of its best known substrates.
The 24 tandem ankyrin repeats are responsible for the recognition of a wide range of membrane proteins. These 24 repeats contain 3 structurally distinct binding sites ranging from repeat 1-14.